The stimulatory effect of luteinizing hormone on adenosine 3',5'-monophosphate accumulation in corpus luteum slices.
نویسندگان
چکیده
The presence of adenosine 3’,5’-monophosphate was demonstrated in bovine luteal tissue. The addition of luteinizing hormone to incubating slices of a bovine corpus luteum caused a rapid accumulation of this cyclic nucleotide which preceded the increase in progesterone synthesis. This effect appeared to be specific for luteinizing hormone. Puromycin did not inhibit this action of luteinizing hormone on cyclic AMP accumulation. In view of the previous finding that exogenous cyclic AMP added to incubating slices can mimic the effect of luteinizing hormone on steroidogenesis, these results indicate that the cyclic nucleotide is a mediator of this action of luteinizing hormone. An increase in the concentration of cyclic AMP has also been demonstrated in a human corpus luteum stimulated in vifro by human chorionic gonadotropin.
منابع مشابه
Cyclic adenosine 3',5'-monophosphate and luteinizing hormone stimulated protein kinase from bovine corpus luteum: evidence for activation through separate mechanisms.
Protein kinases catalyze the transfer of the terminal phosphate of ATP to a variety of acceptor proteins [ 11. It has been demonstrated that cyclic adenosine 3’, 5’-monophosphate (cyclic AMP) activates protein kinase (holoenzyme, RC) by forming a complex with the regulatory subunit (R) to release the catalytic subunit (C) in the active state [2,3]. In a previous communication from this laborato...
متن کاملPurification and Properties of a Protein Kinase from Bovine Corpus Luteum That Is Stimulated by Cyclic Adenosine 3’ ,5’-Monophosphate and Luteinizing Hormone*
A protein kinase has been purified from the bovine corpus luteum by acid precipitation, ammonium sulfate fractionation and chromatography on DEAE-cellulose and hydroxylapatite columns. The enzyme has a molecular weight of approximately 159,000. DEAE-cellulose chromatography resolved the protein kinase activity into two peaks, designated as KI and KII. Both peaks possessed adenosine 3’,5’-monoph...
متن کاملStimulatory effect of gonadotropins on the synthesis of adenosine 3': 5'-cyclic monophosphate and progesterone by suspensions of rat ovarian interstitial cells.
A cell suspension was prepared from immature rat ovaries by treatment with trypsin and collagenase. The isolated cells were capable of converting [8-14-C]adenine to cyclic [-14-C]AMP and the rate of this conversion was stimulated in vitro by luteinizing hormone and human chorionic gonadotropine, but not by prolactin, norepinephrine, dopamine or albumin. The accumulation of progesterone was al...
متن کاملPurification and properties of a protein kinase from bovine corpus luteum that is stimulated by cyclic adenosine 3',5'-monophosphate and luteinizing hormone.
A protein kinase has been purified from the bovine corpus luteum by acid precipitation, ammonium sulfate fractionation and chromatography on DEAE-cellulose and hydroxylapatite columns. The enzyme has a molecular weight of approximately 159,000. DEAE-cellulose chromatography resolved the protein kinase activity into two peaks, designated as KI and KII. Both peaks possessed adenosine 3’,5’-monoph...
متن کاملPurification and Properties of a Protein Kinase from Bovine Corpus Luteum That Is Stimulated by Cyclic Adenosine 3’ ,5’-Monophosphate and Luteinizing Hormone*
A protein kinase has been purified from the bovine corpus luteum by acid precipitation, ammonium sulfate fractionation and chromatography on DEAE-cellulose and hydroxylapatite columns. The enzyme has a molecular weight of approximately 159,000. DEAE-cellulose chromatography resolved the protein kinase activity into two peaks, designated as KI and KII. Both peaks possessed adenosine 3’,5’-monoph...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 241 22 شماره
صفحات -
تاریخ انتشار 1966